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Serum IgA reactivity against GroEL of Streptococcus sanguinis and human heterogeneous nuclear ribonucleoprotein A2/B1 in patients with Behçet disease
Author(s) -
Cho S.B.,
Zheng Z.,
Ahn K.J.,
Choi M.J.,
Cho S.,
Kim D.Y.,
Lee H.S.,
Bang D.
Publication year - 2013
Publication title -
british journal of dermatology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.304
H-Index - 179
eISSN - 1365-2133
pISSN - 0007-0963
DOI - 10.1111/bjd.12128
Subject(s) - groel , epitope , streptococcus sanguinis , virology , heterogeneous nuclear ribonucleoprotein , biology , epitope mapping , recombinant dna , antibody , microbiology and biotechnology , ribonucleoprotein , immunology , escherichia coli , gene , biochemistry , genetics , bacteria , streptococcus mutans , rna
Summary Background Infectious agents, especially Streptococcus sanguinis and herpes simplex virus, have long been postulated as major triggering factors for Behçet disease (BD). Objectives To identify an anti‐ S. sanguinis antigen reacting with serum IgA antibody in patients with BD. Methods We detected a target protein by proteomics analysis and evaluated serum IgA reactivity of 100 patients with BD against the identified streptococcal target protein and human heterogeneous nuclear ribonucleoprotein (hnRNP) A2/B1. Homologous epitope sequences between the streptococcal target protein and human hnRNP A2/B1 were also evaluated. Results Four protein bands were detected by immunoprecipitation, and chaperonin GroEL was identified by a proteomics analysis. Reactivity of serum IgA against recombinant S. sanguinis GroEL was detected in 77 of 100 patients with BD (77%) and in 21 of 70 healthy controls (30%). In addition, reactivity of serum IgA against human recombinant hnRNP A2/B1 was seen in 79 of 100 patients with BD (79%) and in eight of 70 healthy controls (11%). Among the eight distinctive epitopes with significant homology between S. sanguinis GroEL and human hnRNP A2/B1, the serum IgA reactivity of patients with BD was markedly higher with epitope 3 (hnRNP A2/B1 peptide 33–46 and GroEL peptide 57–70) and epitope 6 (hnRNP A2/B1 peptide 177–188 and GroEL peptide 347–358). Conclusion We identified an S. sanguinis GroEL protein as a target of serum anti‐ S. sanguinis IgA antibody reactivity in patients with BD. In addition, patients with BD exhibited serum IgA reactivity against homologous epitope regions between S. sanguinis GroEL and human hnRNP A2/B1.